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Vol. 15, Issue 2, 637-648, February 2004
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* Washington University School of Medicine, Department of Cell Biology and Physiology, St. Louis, Missouri 63110;
University of North Carolina, Department of Cell and Developmental Biology, Chapel Hill, North Carolina 27599
Submitted February 21, 2003;
Revised October 17, 2003;
Accepted October 20, 2003
Monitoring Editor: Benjamin Glick
NSF and p97 are related AAA proteins implicated in membrane trafficking and organelle biogenesis. p97 is also involved in pathways that lead to ubiquitin-dependent proteolysis, including ER-associated degradation (ERAD). In this study, we have used dominant interfering ATP-hydrolysis deficient mutants (NSF(E329Q) and p97(E578Q)) to compare the function of these AAA proteins in the secretory pathway of mammalian cells. Expressing NSF(E329Q) promotes disassembly of Golgi stacks into dispersed vesicular structures. It also rapidly inhibits glycosaminoglycan sulfation, reflecting disruption of intra-Golgi transport. In contrast, expressing p97(E578Q) does not affect Golgi structure or function; glycosaminoglycans are normally sulfated and secreted, as is the VSV-G ts045 protein. Instead, expression of p97(E578Q) causes ubiquitinated proteins to accumulate on ER membranes and slows degradation of the ERAD substrate cystic-fibrosis transmembrane-conductance regulator. In addition, expression of p97(E578Q) eventually causes the ER to swell. More specific assessment of effects of p97(E578Q) on organelle assembly shows that the Golgi apparatus disperses and reassembles normally after treatment with brefeldin A and during mitosis. These findings demonstrate that ATP-hydrolysis-dependent activities of NSF and p97 in the cell are not equivalent and suggest that only NSF is directly involved in regulating membrane fusion.
Abbreviations used: AAA, ATPases associated with a variety of cellular activities; 
-SNAP, soluble NSF attachment protein; GAGs, glycosaminoglycans; SNARE, SNAP receptor.
Corresponding author. E-mail address: phanson{at}cellbiology.wustl.edu.
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